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Database: UniProt
Entry: A0A2K6GMR8_PROCO
LinkDB: A0A2K6GMR8_PROCO
Original site: A0A2K6GMR8_PROCO 
ID   A0A2K6GMR8_PROCO        Unreviewed;       608 AA.
AC   A0A2K6GMR8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE            EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN   Name=PLCZ1 {ECO:0000313|Ensembl:ENSPCOP00000027502.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000027502.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000027502.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: The production of the second messenger molecules
CC       diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated
CC       by activated phosphatidylinositol-specific phospholipase C enzymes. In
CC       vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)-dependent manner. Triggers
CC       intracellular Ca(2+) oscillations in oocytes solely during M phase and
CC       is involved in inducing oocyte activation and initiating embryonic
CC       development up to the blastocyst stage. Is therefore a strong candidate
CC       for the egg-activating soluble sperm factor that is transferred from
CC       the sperm into the egg cytoplasm following gamete membrane fusion. May
CC       exert an inhibitory effect on phospholipase-C-coupled processes that
CC       depend on calcium ions and protein kinase C, including CFTR trafficking
CC       and function. {ECO:0000256|ARBA:ARBA00003992}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC         bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-
CC         diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456,
CC         ChEBI:CHEBI:203600; EC=3.1.4.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00023674};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC         Evidence={ECO:0000256|ARBA:ARBA00023674};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000256|ARBA:ARBA00004556}.
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DR   AlphaFoldDB; A0A2K6GMR8; -.
DR   STRING; 379532.ENSPCOP00000027502; -.
DR   Ensembl; ENSPCOT00000038326.1; ENSPCOP00000027502.1; ENSPCOG00000026247.1.
DR   GeneTree; ENSGT00940000159950; -.
DR   OMA; YLTCTLV; -.
DR   Proteomes; UP000233160; Unplaced.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0045120; C:pronucleus; IEA:Ensembl.
DR   GO; GO:0061827; C:sperm head; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:Ensembl.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR   GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IEA:Ensembl.
DR   GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0060470; P:positive regulation of cytosolic calcium ion concentration involved in egg activation; IEA:Ensembl.
DR   CDD; cd00275; C2_PLC_like; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR001192; PI-PLC_fam.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR015359; PLC_EF-hand-like.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR   PANTHER; PTHR10336:SF29; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE ZETA-1; 1.
DR   PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF09279; EF-hand_like; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   4: Predicted;
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   Fertilization {ECO:0000256|ARBA:ARBA00023279};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361133};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|RuleBase:RU361133};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU361133};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   DOMAIN          35..70
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          349..465
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          465..589
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          306..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   608 AA;  70637 MW;  30B24F86D34244DB CRC64;
     LETKWFWSKI QDEFRGGKIN LEKTQKLLEK LDIPCNIIHV KHIFKDNDRL KQGRITIEEF
     RAIYRTIAHR EEIIEIFNAY SENRKILLEN NLVQFLRQEQ YISEMSKTIA IEIIQKYEPI
     DEVRKEQQMS FEGFTRYMDS PECLLFKHEC RRVYQDMTRP LNDYFISSSH NTYLISDQLV
     GPSDIWGYVS ALVRGCRCLE IDCWDGAQNE PVVYHGYTLT SKLLFKTVLQ AIHKYAFMTS
     DYPVVLSLEN HCSPSQQEVM ADNLQTTFGE SLLADILDDY PDKLPSPEAL KFKILVKNKK
     IGTLKETHER KGSDKHEDNQ DKETESKKAI SAMLFKKKKT RKLKIALALS DLVIYTKAEK
     FRSFQHSRLY QQFNENNSIG ETRARKLSKL KVQEFILHTR KFLTRIYPKA TRADSSNFNP
     QEFWNIGCQM VALNFQTPGL PMDLQNGKFL DNGASGYILK PQFLRDAKSN FNPNKITDSD
     PTTLTIRLIS GIQLPLNNAS SNKADTSVII EVFGVPNDQT KQQTRVIKKN AFSPRWNETF
     TFIIHVPELA LIRFVVENQG LITGNEFLGQ YTIPLLCMNK GYRRVPLFSR MGESLEPASL
     FIYVWYVQ
//
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